Studi Interaksi Molekul Histamin terhadap Protein D7 dari Kelenjar Saliva AE. Aegypti sebagai Agen Baru Anti Inflamasi

Abstract

Mosquito salivary glands are paired-structured organs that have components in the form of D7 protein that plays an important role in the blood-feeding process. D7 protein is able to modulate the host's immune response by binding to various compounds, including histamine compounds that play a role in inflammatory mediators. This study was conducted using the molecular docking method to analyze the interaction between D7 protein and human histamine ligands. The interaction of D7 protein with human histamine ligands has the potential to modulate anti-inflammatory responses in the host body. Molecular docking validation was carried out by re-docking the native LNR ligand to ensure binding accuracy. The results of molecular docking showed that D7 protein has a strong affinity for histamine compounds with a Gibbs free energy (ΔG) value of -6.56 kcal/mol, indicating a stable and spontaneous interaction. The bond that occurs in the interaction of D7 protein and histamine ligand is a conventional hydrogen bond, which plays a major role in the stability and spontaneity of the interaction. Amino acid residues found to bind to the active site of D7 protein and interact with atoms on the histamine ligand include Glutamine 158 (GLU 158), Isoleucine 175 (ILE 175), Tyrosine 178 (TYR 178), Aspartic Acid 265 (ASP 265), and Glutamine 268 (GLU 268). This study supports further understanding of the potential ability of D7 protein as an anti-inflammatory agent during the mosquito blood-feeding process.